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Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins

Fedorov, R V; Meshcheryakov, V A; Gongadze, G M; Fomenkova, N P; Nevskaya N A, N A; Selmer, Maria LU ; Laurberg, Martin LU ; Kristensen, Ole; Al-Karadaghi, Salam LU and Liljas, Anders LU , et al. (2001) In Acta Crystallographica. Section D: Biological Crystallography D57(7). p.968-976
Abstract
The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the... (More)
The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5. (Less)
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keywords
general stress protein CTC, protein-RNA complex, cadmium ions
in
Acta Crystallographica. Section D: Biological Crystallography
volume
D57
issue
7
pages
968 - 976
publisher
John Wiley and Sons Inc.
external identifiers
  • scopus:14344278877
ISSN
1399-0047
language
English
LU publication?
yes
id
5c6def91-6403-4fd9-9678-7d267885992d (old id 948781)
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http://www.blackwell-synergy.com/doi/abs/10.1107/S0907444901006291
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2008-01-24 17:52:31
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2018-05-29 10:09:16
@article{5c6def91-6403-4fd9-9678-7d267885992d,
  abstract     = {The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 Å resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven -strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd2+ ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5.},
  author       = {Fedorov, R V and Meshcheryakov, V A and Gongadze, G M and Fomenkova, N P and Nevskaya N A, N A and Selmer, Maria and Laurberg, Martin and Kristensen, Ole and Al-Karadaghi, Salam and Liljas, Anders and Garber, Marina and Nikonov, S},
  issn         = {1399-0047},
  keyword      = {general stress protein CTC,protein-RNA complex,cadmium ions},
  language     = {eng},
  number       = {7},
  pages        = {968--976},
  publisher    = {John Wiley and Sons Inc.},
  series       = {Acta Crystallographica. Section D: Biological Crystallography},
  title        = {Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins},
  volume       = {D57},
  year         = {2001},
}